Refined structure of dienelactone hydrolase at 1.8 A.
Refined structure of dienelactone hydrolase at 1.8 A.
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1.8 A 下二烯内酯水解酶的精细结构。
DOI：
10.1016/0022-2836(90)90196-s
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发表时间：
1990
影响因子：
5.6
通讯作者：
David L. Ollis
中科院分区：
文献类型：
--
作者：
D. Pathak;David L. Ollis
本文报道了假单胞菌B13双烯内酯水解酶（DLH）的结构。DLH的最终分子模型具有0.150的conventionalR值，并且包括除了羧基末端三个晶体学上无序的残基之外的所有残基。最终模型中包含了279个水分子的位置。该模型与理想键距的均方根偏差为0.014 A，原子坐标的误差估计为0.15 A。DLH是一种含有236个氨基酸残基的单体酶，是细菌和真菌中发现的β-酮己二酸途径的成员。DLH是一种α/β蛋白，含有7个螺旋和8条β折叠片层。可见单个4圈310螺旋。活性位点Cys 123位于α-螺旋的N-末端，其独特之处在于其完全由疏水残基组成（C-末端赖氨酸除外）。β折叠由平行链组成，但链2除外，其在中心β折叠的N末端产生短的反平行区域。活性位点半胱氨酸残基是由Cys 123、His 202和Asp 171组成的残基三联体的一部分，并且使人联想到丝氨酸/半胱氨酸蛋白酶。与木瓜蛋白酶和猕猴桃蛋白酶一样，活性硫醇在X射线数据收集过程中被部分氧化。描述了还原硫和氧化硫的位置。活性位点的几何形状表明，在天然硫醇的构象发生变化后，扩散到DLH的活性位点裂缝的基板。这使得γ-硫的亲核攻击能够通过开环反应发生在环酯底物上。
The structure of dienelactone hydrolase (DLH) fromPseudomonus sp. B13, after stereochemically restrained least-squares refinement at 1.8A˚resolution, is described. The final molecular model of DLH has a conventionalRvalue of 0.150 and includes all but the car☐yl-terminal three residues that are crystallographically disordered. The positions of 279 water molecules are included in the final model. The root-mean-square deviation from ideal bond distances for the model is 0.014A˚and the error in atomic co-ordinates is estimated to be 0.15A˚. DLH is a monomeric enzyme containing 236 amino acid residues and is a member of the β-ketoadipate pathway found in bacteria and fungi. DLH is an α/β protein containing seven helices and eight strands of β-pleated sheet. A single 4-turn 310-helix is seen. The active-site Cys123 resides at the N-terminal end of an α-helix that is peculiar in its consisting entirely of hydrophobic residues (except for a C-terminal lysine). The β-sheet is composed of parallel strands except for strand 2, which gives rise to a short antiparallel region at the N-terminal end of the central β-sheet. The active-site cysteine residue is part of a triad of residues consisting of Cys123, His202 and Asp171, and is reminiscent of the serine/cysteine proteases. As in papain and actinidin, the active thiol is partially oxidized during X-ray data collection. The positions of both the reduced and the oxidized sulphur are described. The active site geometry suggests that a change in the conformation of the native thiol occurs upon diffusion of substrate into the active site cleft of DLH. This enables nucleophilic attack by the γ-sulphur to occur on the cyclic ester substrate through a ring-opening reaction.
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影响因子：
56.9
作者：
ROSE, GD;GESELOWITZ, AR;ZEHFUS, MH
通讯作者：
ZEHFUS, MH
用于带有多线区域检测器的衍射仪的软件。
影响因子：
--
作者：
Howard,AJ;Nielsen,C;Xuong,NH
通讯作者：
Xuong,NH
影响因子：
56.9
作者：
SUNDARALINGAM, M;SEKHARUDU, YC
通讯作者：
SEKHARUDU, YC
使用聚焦成像正比计数器进行蛋白质、DNA 和病毒晶体学分析。
DOI：
10.1126/science.3704639
发表时间：
1986
期刊：
Science (New York, N.Y.)
影响因子：
--
作者：
Durbin,RM;Burns,R;Moulai,J;Metcalf,P;Freymann,D;Blum,M;Anderson,JE;Harrison,SC;Wiley,DC
通讯作者：
Wiley,DC
酶的晶体与溶液结构：结晶丝氨酸蛋白酶的核磁共振波谱。
DOI：
10.1126/science.2499045
发表时间：
1989
期刊：
Science (New York, N.Y.)
影响因子：
--
作者：
Smith,SO;Farr-Jones,S;Griffin,RG;Bachovchin,WW
通讯作者：
Bachovchin,WW